2cpk
From Proteopedia
(New page: 200px<br /><applet load="2cpk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cpk, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:2cpk.gif|left|200px]]<br /><applet load="2cpk" size=" | + | [[Image:2cpk.gif|left|200px]]<br /><applet load="2cpk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2cpk, resolution 2.7Å" /> | caption="2cpk, resolution 2.7Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE'''<br /> | '''CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the catalytic subunit of cyclic adenosine | + | The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 A resolution to an R factor of 0.212. The magnesium adenosine triphosphate (MgATP) binding site was located by difference Fourier synthesis. The enzyme structure is bilobal with a deep cleft between the lobes. The cleft is filled by MgATP and a portion of the inhibitor peptide. The smaller lobe, consisting mostly of amino-terminal sequence, is associated with nucleotide binding, and its largely antiparallel beta sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single beta sheet at the domain interface. This lobe is primarily involved in peptide binding and catalysis. Residues 40 through 280 constitute a conserved catalytic core that is shared by more than 100 protein kinases. Most of the invariant amino acids in this conserved catalytic core are clustered at the sites of nucleotide binding and catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 2CPK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with PO3 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 2CPK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=PO3:'>PO3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1CPK. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CPK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Ashford, V | + | [[Category: Ashford, V A.]] |
| - | [[Category: Knighton, D | + | [[Category: Knighton, D R.]] |
| - | [[Category: Sowadski, J | + | [[Category: Sowadski, J M.]] |
| - | [[Category: Taylor, S | + | [[Category: Taylor, S S.]] |
| - | [[Category: Teneyck, L | + | [[Category: Teneyck, L F.]] |
| - | [[Category: Xuong, N | + | [[Category: Xuong, N H.]] |
[[Category: Zheng, J.]] | [[Category: Zheng, J.]] | ||
[[Category: PO3]] | [[Category: PO3]] | ||
[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:51:16 2008'' |
Revision as of 14:51, 21 February 2008
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CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE
Overview
The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 A resolution to an R factor of 0.212. The magnesium adenosine triphosphate (MgATP) binding site was located by difference Fourier synthesis. The enzyme structure is bilobal with a deep cleft between the lobes. The cleft is filled by MgATP and a portion of the inhibitor peptide. The smaller lobe, consisting mostly of amino-terminal sequence, is associated with nucleotide binding, and its largely antiparallel beta sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single beta sheet at the domain interface. This lobe is primarily involved in peptide binding and catalysis. Residues 40 through 280 constitute a conserved catalytic core that is shared by more than 100 protein kinases. Most of the invariant amino acids in this conserved catalytic core are clustered at the sites of nucleotide binding and catalysis.
About this Structure
2CPK is a Protein complex structure of sequences from Mus musculus with as ligand. This structure supersedes the now removed PDB entry 1CPK. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase., Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, Sowadski JM, Science. 1991 Jul 26;253(5018):407-14. PMID:1862342
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